MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line
- Autores
- Buitrago, Claudia Graciela; Ronda, Ana Carolina; Russo, Ana Josefa; Boland, Ricardo Leopoldo
- Año de publicación
- 2006
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In chick skeletal muscle cell primary cultures, we previously demonstrated that 1α,25(OH)2-vitamin D3 [1α,25(OH) 2D3], the hormonally active form of vitamin D, increases the phosphorylation and activity of the extracellular signal-regulated mitogen-activated protein (MAP) kinase isoforms ERK1 and ERK2, their subsequent translocation to the nucleus and involvement in DNA synthesis stimulation. In this study, we show that other members of the MAP kinase superfamily are also activated by the hormone. Using the muscle cell line C2C12 we found that 1α,25(OH)2D3 within 1 min phosphorylates and increases the activity of p38 MAPK. The immediately upstream mitogen-activated protein kinase kinases 3/6 (MKK3/MKK6) were also phosphorylated by the hormone suggesting their participation in p38 activation. 1α,25(OH) 2D3 was able to dephosphorylate/activate the ubiquitous cytosolic tyrosine kinase c-Src in C2C12 cells and studies with specific inhibitors imply that Src participates in hormone induced-p38 activation. Of relevance, 1α,25(OH)2D3 induced in the C2C12 line the stimulation of mitogen-activated protein kinase activating protein kinase 2 (MAPKAP-kinase 2) and subsequent phosphorylation of heat shock protein 27 (HSP27) in a p38 kinase activation-dependent manner. Treatment with the p38 inhibitor, SB203580, blocked p38 phosphorylation caused by the hormone and inhibited the phosphorylation of its downstrean substrates. 1α,25(OH) 2D3 also promotes the phosphorylation of c-jun N-terminal protein kinases (JNK 1/2), the response is fast (0.5-1 min) and maximal phosphorylation of the enzyme is observed at physiological doses of 1α,25(OH)2D3 (1 nM). The relative contribution of ERK-1/2, p38, and JNK-1/2 and their interrelationships in hormonal regulation of muscle cell proliferation and differentiation remain to be established.
Fil: Buitrago, Claudia Graciela. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina
Fil: Ronda, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Russo, Ana Josefa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Fil: Boland, Ricardo Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina - Materia
-
1α,25(OH)2D3
C-SRC
C2C12 CELLS
JNK
MUSCLE
NON-GENOMIC ACTIONS
P38 MAPK - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/94819
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MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell lineBuitrago, Claudia GracielaRonda, Ana CarolinaRusso, Ana JosefaBoland, Ricardo Leopoldo1α,25(OH)2D3C-SRCC2C12 CELLSJNKMUSCLENON-GENOMIC ACTIONSP38 MAPKhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1In chick skeletal muscle cell primary cultures, we previously demonstrated that 1α,25(OH)2-vitamin D3 [1α,25(OH) 2D3], the hormonally active form of vitamin D, increases the phosphorylation and activity of the extracellular signal-regulated mitogen-activated protein (MAP) kinase isoforms ERK1 and ERK2, their subsequent translocation to the nucleus and involvement in DNA synthesis stimulation. In this study, we show that other members of the MAP kinase superfamily are also activated by the hormone. Using the muscle cell line C2C12 we found that 1α,25(OH)2D3 within 1 min phosphorylates and increases the activity of p38 MAPK. The immediately upstream mitogen-activated protein kinase kinases 3/6 (MKK3/MKK6) were also phosphorylated by the hormone suggesting their participation in p38 activation. 1α,25(OH) 2D3 was able to dephosphorylate/activate the ubiquitous cytosolic tyrosine kinase c-Src in C2C12 cells and studies with specific inhibitors imply that Src participates in hormone induced-p38 activation. Of relevance, 1α,25(OH)2D3 induced in the C2C12 line the stimulation of mitogen-activated protein kinase activating protein kinase 2 (MAPKAP-kinase 2) and subsequent phosphorylation of heat shock protein 27 (HSP27) in a p38 kinase activation-dependent manner. Treatment with the p38 inhibitor, SB203580, blocked p38 phosphorylation caused by the hormone and inhibited the phosphorylation of its downstrean substrates. 1α,25(OH) 2D3 also promotes the phosphorylation of c-jun N-terminal protein kinases (JNK 1/2), the response is fast (0.5-1 min) and maximal phosphorylation of the enzyme is observed at physiological doses of 1α,25(OH)2D3 (1 nM). The relative contribution of ERK-1/2, p38, and JNK-1/2 and their interrelationships in hormonal regulation of muscle cell proliferation and differentiation remain to be established.Fil: Buitrago, Claudia Graciela. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; ArgentinaFil: Ronda, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaFil: Russo, Ana Josefa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaFil: Boland, Ricardo Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; ArgentinaWiley-liss, Div John Wiley & Sons Inc2006-03-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/94819Buitrago, Claudia Graciela; Ronda, Ana Carolina; Russo, Ana Josefa; Boland, Ricardo Leopoldo; MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line; Wiley-liss, Div John Wiley & Sons Inc; Journal of Cellular Biochemistry; 97; 4; 7-3-2006; 698-7080730-2312CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jcb.20639info:eu-repo/semantics/altIdentifier/doi/10.1002/jcb.20639info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:49:08Zoai:ri.conicet.gov.ar:11336/94819instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:49:08.83CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
title |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
spellingShingle |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line Buitrago, Claudia Graciela 1α,25(OH)2D3 C-SRC C2C12 CELLS JNK MUSCLE NON-GENOMIC ACTIONS P38 MAPK |
title_short |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
title_full |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
title_fullStr |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
title_full_unstemmed |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
title_sort |
MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line |
dc.creator.none.fl_str_mv |
Buitrago, Claudia Graciela Ronda, Ana Carolina Russo, Ana Josefa Boland, Ricardo Leopoldo |
author |
Buitrago, Claudia Graciela |
author_facet |
Buitrago, Claudia Graciela Ronda, Ana Carolina Russo, Ana Josefa Boland, Ricardo Leopoldo |
author_role |
author |
author2 |
Ronda, Ana Carolina Russo, Ana Josefa Boland, Ricardo Leopoldo |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
1α,25(OH)2D3 C-SRC C2C12 CELLS JNK MUSCLE NON-GENOMIC ACTIONS P38 MAPK |
topic |
1α,25(OH)2D3 C-SRC C2C12 CELLS JNK MUSCLE NON-GENOMIC ACTIONS P38 MAPK |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
In chick skeletal muscle cell primary cultures, we previously demonstrated that 1α,25(OH)2-vitamin D3 [1α,25(OH) 2D3], the hormonally active form of vitamin D, increases the phosphorylation and activity of the extracellular signal-regulated mitogen-activated protein (MAP) kinase isoforms ERK1 and ERK2, their subsequent translocation to the nucleus and involvement in DNA synthesis stimulation. In this study, we show that other members of the MAP kinase superfamily are also activated by the hormone. Using the muscle cell line C2C12 we found that 1α,25(OH)2D3 within 1 min phosphorylates and increases the activity of p38 MAPK. The immediately upstream mitogen-activated protein kinase kinases 3/6 (MKK3/MKK6) were also phosphorylated by the hormone suggesting their participation in p38 activation. 1α,25(OH) 2D3 was able to dephosphorylate/activate the ubiquitous cytosolic tyrosine kinase c-Src in C2C12 cells and studies with specific inhibitors imply that Src participates in hormone induced-p38 activation. Of relevance, 1α,25(OH)2D3 induced in the C2C12 line the stimulation of mitogen-activated protein kinase activating protein kinase 2 (MAPKAP-kinase 2) and subsequent phosphorylation of heat shock protein 27 (HSP27) in a p38 kinase activation-dependent manner. Treatment with the p38 inhibitor, SB203580, blocked p38 phosphorylation caused by the hormone and inhibited the phosphorylation of its downstrean substrates. 1α,25(OH) 2D3 also promotes the phosphorylation of c-jun N-terminal protein kinases (JNK 1/2), the response is fast (0.5-1 min) and maximal phosphorylation of the enzyme is observed at physiological doses of 1α,25(OH)2D3 (1 nM). The relative contribution of ERK-1/2, p38, and JNK-1/2 and their interrelationships in hormonal regulation of muscle cell proliferation and differentiation remain to be established. Fil: Buitrago, Claudia Graciela. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina Fil: Ronda, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Russo, Ana Josefa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Boland, Ricardo Leopoldo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina |
description |
In chick skeletal muscle cell primary cultures, we previously demonstrated that 1α,25(OH)2-vitamin D3 [1α,25(OH) 2D3], the hormonally active form of vitamin D, increases the phosphorylation and activity of the extracellular signal-regulated mitogen-activated protein (MAP) kinase isoforms ERK1 and ERK2, their subsequent translocation to the nucleus and involvement in DNA synthesis stimulation. In this study, we show that other members of the MAP kinase superfamily are also activated by the hormone. Using the muscle cell line C2C12 we found that 1α,25(OH)2D3 within 1 min phosphorylates and increases the activity of p38 MAPK. The immediately upstream mitogen-activated protein kinase kinases 3/6 (MKK3/MKK6) were also phosphorylated by the hormone suggesting their participation in p38 activation. 1α,25(OH) 2D3 was able to dephosphorylate/activate the ubiquitous cytosolic tyrosine kinase c-Src in C2C12 cells and studies with specific inhibitors imply that Src participates in hormone induced-p38 activation. Of relevance, 1α,25(OH)2D3 induced in the C2C12 line the stimulation of mitogen-activated protein kinase activating protein kinase 2 (MAPKAP-kinase 2) and subsequent phosphorylation of heat shock protein 27 (HSP27) in a p38 kinase activation-dependent manner. Treatment with the p38 inhibitor, SB203580, blocked p38 phosphorylation caused by the hormone and inhibited the phosphorylation of its downstrean substrates. 1α,25(OH) 2D3 also promotes the phosphorylation of c-jun N-terminal protein kinases (JNK 1/2), the response is fast (0.5-1 min) and maximal phosphorylation of the enzyme is observed at physiological doses of 1α,25(OH)2D3 (1 nM). The relative contribution of ERK-1/2, p38, and JNK-1/2 and their interrelationships in hormonal regulation of muscle cell proliferation and differentiation remain to be established. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-03-07 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/94819 Buitrago, Claudia Graciela; Ronda, Ana Carolina; Russo, Ana Josefa; Boland, Ricardo Leopoldo; MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line; Wiley-liss, Div John Wiley & Sons Inc; Journal of Cellular Biochemistry; 97; 4; 7-3-2006; 698-708 0730-2312 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/94819 |
identifier_str_mv |
Buitrago, Claudia Graciela; Ronda, Ana Carolina; Russo, Ana Josefa; Boland, Ricardo Leopoldo; MAP kinases p38 and JNK are activated by the steroid hormone 1α,25(OH)2-vitamin D3 in the C2C12 muscle cell line; Wiley-liss, Div John Wiley & Sons Inc; Journal of Cellular Biochemistry; 97; 4; 7-3-2006; 698-708 0730-2312 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jcb.20639 info:eu-repo/semantics/altIdentifier/doi/10.1002/jcb.20639 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Wiley-liss, Div John Wiley & Sons Inc |
publisher.none.fl_str_mv |
Wiley-liss, Div John Wiley & Sons Inc |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1844613523140771840 |
score |
13.070432 |